ID   SYE_XANC8               Reviewed;         467 AA.
AC   Q4UWS6;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   10-JUN-2026, entry version 107.
DE   RecName: Full=Glutamate--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00022};
DE            EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00022};
DE   AltName: Full=Glutamyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00022};
DE            Short=GluRS {ECO:0000255|HAMAP-Rule:MF_00022};
GN   Name=gltX {ECO:0000255|HAMAP-Rule:MF_00022};
GN   OrderedLocusNames=XC_1429;
OS   Xanthomonas campestris pv. campestris (strain 8004).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Lysobacterales; Lysobacteraceae; Xanthomonas.
OX   NCBI_TaxID=314565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8004;
RX   PubMed=15899963; DOI=10.1101/gr.3378705;
RA   Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA   Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S.,
RA   Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., Fang R.,
RA   Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT   "Comparative and functional genomic analyses of the pathogenicity of
RT   phytopathogen Xanthomonas campestris pv. campestris.";
RL   Genome Res. 15:757-767(2005).
CC   -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-
CC       step reaction: glutamate is first activated by ATP to form Glu-AMP and
CC       then transferred to the acceptor end of tRNA(Glu). {ECO:0000255|HAMAP-
CC       Rule:MF_00022}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Glu) + L-glutamate + ATP = L-glutamyl-tRNA(Glu) + AMP +
CC         diphosphate; Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663, Rhea:RHEA-
CC         COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78520, ChEBI:CHEBI:456215;
CC         EC=6.1.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_00022};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00022}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00022}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       Glutamate--tRNA ligase type 1 subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00022}.
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DR   EMBL; CP000050; AAY48497.1; -; Genomic_DNA.
DR   RefSeq; WP_011037816.1; NC_007086.1.
DR   AlphaFoldDB; Q4UWS6; -.
DR   SMR; Q4UWS6; -.
DR   KEGG; xcb:XC_1429; -.
DR   HOGENOM; CLU_015768_6_3_6; -.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00808; GluRS_core; 1.
DR   FunFam; 3.40.50.620:FF:000007; Glutamate--tRNA ligase; 1.
DR   Gene3D; 1.10.10.350; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00022; Glu_tRNA_synth_type1; 1.
DR   InterPro; IPR045462; aa-tRNA-synth_I_cd-bd.
DR   InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR   InterPro; IPR004527; Glu-tRNA-ligase_bac/mito.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR049940; GluQ/Sye.
DR   InterPro; IPR033910; GluRS_core.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00464; gltX_bact; 1.
DR   PANTHER; PTHR43311; GLUTAMATE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43311:SF2; GLUTAMATE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF19269; Anticodon_2; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF48163; An anticodon-binding domain of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..467
FT                   /note="Glutamate--tRNA ligase"
FT                   /id="PRO_0000237419"
FT   MOTIF           9..19
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT   MOTIF           237..241
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT   BINDING         240
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
SQ   SEQUENCE   467 AA;  51983 MW;  C9418B1D0D82245F CRC64;
     MTCRTRFAPS PTGYLHIGGA RTALYCWLEA RHRGGQFVLR IEDTDRERST QVAIDAILEA
     MEWLGLGYDE GPIYQTQRIA RYQEVAEQLL AQGKAYYAYE TREELDAMRE AAMAKQEKPR
     YNGAAREQQL PYRDDPNRVI RFKNPLAGTV VFDDLIKGRI EIANSELDDM VIFRPDGYPT
     YNFAVVVDDW DMGITEVIRG DDHINNTPRQ INIYEALGAP VPKFAHMPMI LDEQGAKLSK
     RTGAADVMQY KDAGYLPHAL INYLARLGWS HGDQELFSQQ ELLDLFDVKD VNSKAARLDM
     AKLGWVNQHY LKTDDPASIA PQLEYQLRKL GIDVAAGPAA ADVVVALRER VQTLKEMAEK
     AVVWYQPLET YDEAAVIKHL KLGAEVPLGK AREMLAALNE WSVENVSAAL HAAAAALELG
     MGKVAQPLRV AITGTQVSPD ISQTVYLAGR EGALKRIDAA LIKIGAA
//